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Acta Crystallogr Sect F Struct Biol Cryst Commun. May 1, 2007; 63(Pt 5): 361–368.
Published online Apr 28, 2007. doi:  10.1107/S1744309107019185
PMCID: PMC2334995
Oligomerization of BenM, a LysR-type transcriptional regulator: structural basis for the aggregation of proteins in this family
Obidimma C. Ezezika,a Sandra Haddad,a Ellen L. Neidle,a and Cory Momanyb*
aDepartment of Microbiology, University of Georgia, Athens, GA 30602, USA
bDepartment of Pharmaceutical and Biomedical Sciences, University of Georgia, Athens, GA 30602, USA
Correspondence e-mail: cmomany/at/mail.rx.uga.edu
Current address: Department of Molecular, Cellular and Developmental Biology, Yale University, New Haven, CT 06520, USA.
Received December 11, 2006; Accepted April 17, 2007.
Abstract
LysR-type transcriptional regulators comprise the largest family of homologous regulatory DNA-binding proteins in bacteria. A problematic challenge in the crystallization of LysR-type regulators stems from the insolubility and precipitation difficulties encountered with high concentrations of the full-length versions of these proteins. A general oligomerization scheme is proposed for this protein family based on the structures of the effector-binding domain of BenM in two different space groups, P4322 and C2221. These structures used the same oligomerization scheme of dimer–dimer interactions as another LysR-type regulator, CbnR, the full-length structure of which is available [Muraoka et al. (2003), J. Mol. Biol. 328, 555–566]. Evaluation of packing relationships and surface features suggests that BenM can form infinite oligomeric arrays in crystals through these dimer–dimer interactions. By extrapolation to the liquid phase, such dimer–dimer interactions may contribute to the significant difficulty in crystallizing full-length members of this family. The oligomerization of dimeric units to form biologically important tetramers appears to leave unsatisfied oligomerization sites. Under conditions that favor association, such as neutral pH and concentrations appropriate for crystallization, higher order oligomerization could cause solubility problems with purified proteins. A detailed model by which BenM and other LysR-type transcriptional regulators may form these arrays is proposed.
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International Union of Crystallography